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. 2018 Oct 16;9:2382. doi: 10.3389/fimmu.2018.02382

Figure 3.

Figure 3

Structure of human CRP with bound phosphocholine and bis(phosphocholine)-hexane. (A) Space filling model of “B” face of human CRP with phosphocholine bound in each of the protomer binding sites. (B) 3D X-ray crystal structure of phosphocholine in the binding pocket of a single CRP protomer within the native molecule, showing the ligand interactions with calcium and the CRP residues responsible for binding. (C) The structure of bis(phosphocholine)-hexane (above) and the structure of the complex formed by two CRP molecules cross linked by five bis(phosphocholine)-hexane molecules; face on (left) and side on (right) [From reference (32) with permission of Macmillan Publishers Ltd].